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Protein

AMP deaminase 1

Gene

AMPD1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

AMP deaminase plays a critical role in energy metabolism.

Catalytic activityi

AMP + H2O = IMP + NH3.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathwayi

GO - Molecular functioni

  1. AMP deaminase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. IMP salvage Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00591; UER00663.

Names & Taxonomyi

Protein namesi
Recommended name:
AMP deaminase 1 (EC:3.5.4.6)
Alternative name(s):
AMP deaminase isoform M
Myoadenylate deaminase
Gene namesi
Name:AMPD1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811 Componenti: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›26›26AMP deaminase 1PRO_0000194404Add
BLAST

Expressioni

Tissue specificityi

Three isoforms are present in mammals: AMP deaminase 1 is the predominant form in skeletal muscle; AMP deaminase 2 predominates in smooth muscle, non-muscle tissue, embryonic muscle and undifferentiated myoblasts; AMP deaminase 3 is found in erythrocytes.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000014118.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1816.
InParanoidiP81072.

Family and domain databases

InterProiIPR006329. AMPD.
IPR029770. AMPD1.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PTHR11359:SF1. PTHR11359:SF1. 1 hit.

Sequencei

Sequence statusi: Fragment.

P81072-1 [UniParc]FASTAAdd to basket

« Hide

        10         20 
MNQKHLLRFI KKSYQVDADR VVYSTK
Length:26
Mass (Da):3,169
Last modified:November 1, 1997 - v1
Checksum:iB022467EACBB6E75
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei26 – 261

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000014118.

Chemistry

ChEMBLiCHEMBL2242733.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG1816.
InParanoidiP81072.

Enzyme and pathway databases

UniPathwayiUPA00591; UER00663.

Family and domain databases

InterProiIPR006329. AMPD.
IPR029770. AMPD1.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PTHR11359:SF1. PTHR11359:SF1. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "AMP-deaminases from chicken and rabbit muscle: partial primary sequences of homologous 17-kDa CNBr fragments: autorecognition by rabbit anti-[chicken AMPD]."
    Chilson O.P., Kelly-Chilson A.E., Siegel N.R.
    Comp. Biochem. Physiol. 116B:371-377(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.

Entry informationi

Entry nameiAMPD1_RABIT
AccessioniPrimary (citable) accession number: P81072
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.